ID K6ULM5_9MICO Unreviewed; 290 AA.
AC K6ULM5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative peptidase {ECO:0000313|EMBL:GAB77376.1};
GN ORFNames=AUCHE_05_02850 {ECO:0000313|EMBL:GAB77376.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77376.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB77376.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77376.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB77376.1}.
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DR EMBL; BAGZ01000005; GAB77376.1; -; Genomic_DNA.
DR RefSeq; WP_006502128.1; NZ_BAGZ01000005.1.
DR AlphaFoldDB; K6ULM5; -.
DR STRING; 100225.SAMN05421595_1204; -.
DR eggNOG; COG5640; Bacteria.
DR OrthoDB; 3611234at2; -.
DR Proteomes; UP000008495; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000008495};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..290
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003898519"
FT DOMAIN 43..283
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 290 AA; 30649 MW; BA808BD9BB75916D CRC64;
MKKSTRRMRR FGLLGLAVSM AATLFPTGSQ AAPPSGEEDT AKIIGGVAAS RDEFPFMVSL
QTSRGHFCGG SLYRSTMVLT AAHCVLDIVA DGAGNGVPVS EVTAVIGRTN HSDKNQGVER
KVELREVSKE PRITIHPNHM NQVGFDLAIV HLDKPVTGIA PVRVPTKGTD ALIAPGSMAT
VIGWGNTDTD LGRGTERLRK VDVPILSQEE CLVNADRDIN GEVEICAGRK GKDSCQGDSG
GPLLRKVPGR DEYLQIGVVS RGAGCAAQGG PGIYSYLGSQ LLWRTMGSLG
//
